The goal of this administrative supplement is to acquire an advanced optical tweezers instrument. Capitalizing on the progress made in the previous two years of funding, this instrument will be used to conduct experiments to probe key questions within the scope of the parent grant. These questions include intermediates along binding pathways of intrinsically disordered proteins, conformational dynamics of disordered proteins under macromolecular crowding, and physical properties of protein droplets formed by liquid-liquid phase separation. The instruments complements well the ongoing efforts of the parent grant and will significantly raise the quality and impact of the research.

Public Health Relevance

Molecular recognition is at the core of biology. This administrative supplement for instrument will generate fundamental knowledge on molecular recognition processes occurring at a wide range of spatial scales and yield unique opportunities for drug design through altering mechanistic pathways.

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Unknown (R35)
Project #
3R35GM118091-03S1
Application #
9700280
Study Section
Special Emphasis Panel (ZGM1)
Program Officer
Lyster, Peter
Project Start
2016-04-15
Project End
2021-03-31
Budget Start
2018-04-01
Budget End
2019-03-31
Support Year
3
Fiscal Year
2018
Total Cost
Indirect Cost
Name
University of Illinois at Chicago
Department
Chemistry
Type
Schools of Arts and Sciences
DUNS #
098987217
City
Chicago
State
IL
Country
United States
Zip Code
60612
Zhou, Huan-Xiang; Pang, Xiaodong (2018) Electrostatic Interactions in Protein Structure, Folding, Binding, and Condensation. Chem Rev 118:1691-1741
Nguemaha, Valery; Qin, Sanbo; Zhou, Huan-Xiang (2018) Atomistic Modeling of Intrinsically Disordered Proteins Under Polyethylene Glycol Crowding: Quantitative Comparison with Experimental Data and Implication of Protein-Crowder Attraction. J Phys Chem B :
Hicks, Alan; Zhou, Huan-Xiang (2018) Temperature-induced collapse of a disordered peptide observed by three sampling methods in molecular dynamics simulations. J Chem Phys 149:072313
Zhou, Huan-Xiang; Nguemaha, Valery; Mazarakos, Konstantinos et al. (2018) Why Do Disordered and Structured Proteins Behave Differently in Phase Separation? Trends Biochem Sci 43:499-516
Campitelli, Paul; Guo, Jingjing; Zhou, Huan-Xiang et al. (2018) Hinge-Shift Mechanism Modulates Allosteric Regulations in Human Pin1. J Phys Chem B 122:5623-5629
Amin, Johansen B; Leng, Xiaoling; Gochman, Aaron et al. (2018) A conserved glycine harboring disease-associated mutations permits NMDA receptor slow deactivation and high Ca2+ permeability. Nat Commun 9:3748
Nguemaha, Valery; Zhou, Huan-Xiang (2018) Liquid-Liquid Phase Separation of Patchy Particles Illuminates Diverse Effects of Regulatory Components on Protein Droplet Formation. Sci Rep 8:6728
Nguyen, Trung Hai; Zhou, Huan-Xiang; Minh, David D L (2018) Using the fast fourier transform in binding free energy calculations. J Comput Chem 39:621-636
Banks, Anthony; Qin, Sanbo; Weiss, Kevin L et al. (2018) Intrinsically Disordered Protein Exhibits Both Compaction and Expansion under Macromolecular Crowding. Biophys J 114:1067-1079
Amin, Johansen B; Salussolia, Catherine L; Chan, Kelvin et al. (2017) Divergent roles of a peripheral transmembrane segment in AMPA and NMDA receptors. J Gen Physiol 149:661-680

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